Zobrazeno 1 - 10 of 24 pro vyhledávání: '"M.V. Kryukova"'
1
Akademický článek
Флористические находки в национальном парке «Анюйский» (Хабаровский край)
Autor: M.V. Kryukova
Publikováno v: Turczaninowia, Vol 21, Iss 2, Pp 262-267 (2018)
Приведены сведения о редких, а также находящихся на северных границах распространения видах сосудистых растений, выявленных на террито
Externí odkaz: https://doaj.org/article/b7ddbe53de134a2387e2872bd192bc40
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2
Three-Dimensional Structure of Single-Point Mutant of Esterase PMGL2
Autor: Konstantin M. Boyko, D. A. Goryainova, D. A. Dolgikh, E. A. Kryukova, M.V. Kryukova, Lada E. Petrovskaya, A. Yu. Nikolaeva, D. A. Korzhenevsky
Publikováno v: Crystallography Reports. 66:811-814
Enzymes from extremophilic organisms are of great interest in biotechnology because they possess natural adaptation to extreme conditions often required in biotechnological processes. Lipases are a large class of hydrolytic enzymes, which catalyze th
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::def01ee2143ece2ac8639426e989a8ff
https://doi.org/10.1134/s1063774521050060
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3
Effect of Cysteine Residue Substitution in the GCSAG Motif of the PMGL2 Esterase Active Site on the Enzyme Properties
Autor: D. A. Dolgikh, Alena Yu. Nikolaeva, Konstantin M. Boyko, E. A. Kryukova, S. A. Yakimov, K. A. Novototskaya-Vlasova, Mikhail P. Kirpichnikov, Lada E. Petrovskaya, M.V. Kryukova
Publikováno v: Biochemistry (Moscow). 85:709-716
The gene coding for PMGL2 esterase, which belongs to the family of mammalian hormone-sensitive lipases (HSLs), was discovered by screening a metagenomic DNA library from a permafrost soil. The active site of PMGL2 contains conserved GXSXG motif which
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e722b197ba65b79eb1131791231db7fd
https://doi.org/10.1134/s0006297920060085
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4
Structural and Biochemical Characterization of a Cold-Active PMGL3 Esterase with Unusual Oligomeric Structure
Autor: Konstantin M. Boyko, Alena Yu. Nikolaeva, D. A. Korzhenevsky, K. A. Novototskaya-Vlasova, Dmitry A. Dolgikh, G.Y. Lomakina, Elizaveta Rivkina, Lada E. Petrovskaya, Vladimir Popov, M.V. Kryukova, Mikhail P. Kirpichnikov, E. A. Kryukova
Publikováno v: Biomolecules, Vol 11, Iss 57, p 57 (2021)
Biomolecules
Volume 11
Issue 1
'Biomolecules ', vol: 11, pages: 57-1-57-18 (2021)
The gene coding for a novel cold-active esterase PMGL3 was previously obtained from a Siberian permafrost metagenomic DNA library and expressed in Escherichia coli. We elucidated the 3D structure of the enzyme which belongs to the hormone-sensitive l
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::682b7534240095f9791e4d2d81a1910c
https://www.mdpi.com/2218-273X/11/1/57
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6
Engineering of Thermal Stability in a Cold-Active Oligo-1,6-Glucosidase from Exiguobacterium sibiricum with Unusual Amino Acid Content
Autor: E. A. Kryukova, S. Sh. Gapizov, M.V. Kryukova, Elizaveta Rivkina, Mikhail P. Kirpichnikov, Dmitry A. Dolgikh, Yana Y. Berlina, Lada E. Petrovskaya, L. N. Shingarova
Publikováno v: Biomolecules, Vol 11, Iss 1229, p 1229 (2021)
Biomolecules
Volume 11
Issue 8
A gene coding for a novel putative amylase, oligo-1,6-glucosidase from a psychrotrophic bacterium Exiguobacterium sibiricum from Siberian permafrost soil was cloned and expressed in Escherichia coli. The amino acid sequence of the predicted protein E
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cd8e6876a82d883b7b15aef701fcb8b4
https://doi.org/10.3390/biom11081229
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7
Thermal Inactivation of a Cold-Active Esterase PMGL3 Isolated from the Permafrost Metagenomic Library
Autor: Konstantin M. Boyko, S. A. Yakimov, Eugene G. Maksimov, Lada E. Petrovskaya, Mikhail P. Kirpichnikov, Dmitry A. Dolgikh, Vladimir Popov, M.V. Kryukova, E. A. Kryukova, G. Yu. Lomakina
Publikováno v: Biomolecules
Volume 9
Issue 12
PMGL3 is a cold-adapted esterase which was recently isolated from the permafrost metagenomic library. It exhibits maximum activity at 30 °
C and low stability at elevated temperatures (40 °
C and higher). Sequence alignment has reveal
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::839ad05cba5f5f9f2011837d038dfbc9
https://pubmed.ncbi.nlm.nih.gov/31888238
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8
Akademický článek
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10
Akademický článek
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